Light induced states in MbCO denatured with guanidine hydrochloride.
We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30-80 K. The changes in the Soret band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein.
Natali
F
F
Dipartimento di Fisica, Universita' La Sapienza, Roma, Italy.
Moretti
L
L
Boffi
F
F
Bianconi
A
A
Della Longa
S
S
Congiu Castellano
A
A
D000818:Animals; D002248:Carbon Monoxide / Q000737:chemistry / Q000378:metabolism; D019791:Guanidine / Q000494:pharmacology*; D006736:Horses; D007700:Kinetics; D008027:Light; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism*; D010782:Photolysis; D011489:Protein Denaturation; D013053:Spectrophotometry / Q000379:methods
D009211:Myoglobin; C018013:carboxymyoglobin; D002248:Carbon Monoxide; D019791:Guanidine